5ev9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:33, 10 January 2024) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5ev9 is ON HOLD
+
==Crystal structure of the human BRPF1 bromodomain in complex with SEED15==
 +
<StructureSection load='5ev9' size='340' side='right'caption='[[5ev9]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5ev9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EV9 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5SB:~{N}-[5-(1~{H}-PYRAZOL-4-YL)QUINOLIN-8-YL]ETHANAMIDE'>5SB</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ev9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ev9 OCA], [https://pdbe.org/5ev9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ev9 RCSB], [https://www.ebi.ac.uk/pdbsum/5ev9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ev9 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/BRPF1_HUMAN BRPF1_HUMAN] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Positively regulates the transcription of RUNX1 and RUNX2.<ref>PMID:16387653</ref> <ref>PMID:18794358</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
BRPF1 plays a scaffolding role in transcription. We report on fragment screening by high-throughput docking to the BRPF1 bromodomain which resulted in six chemotypes with very favorable ligand efficiency (0.45-0.50 kcal/mol per non-hydrogen atom). Twenty crystal structures of BRPF1/ligand complexes show structural conservation in the acetyllysine binding site, common binding motifs, and unusual interactions (e.g., the replacement of a conserved water molecule). The structural information is useful for the design of chemical probes.
-
Authors: Zhu, J., Caflisch, A.
+
Twenty Crystal Structures of Bromodomain and PHD Finger Containing Protein 1 (BRPF1)/Ligand Complexes Reveal Conserved Binding Motifs and Rare Interactions.,Zhu J, Caflisch A J Med Chem. 2016 May 24. PMID:27167503<ref>PMID:27167503</ref>
-
Description: Crystal structure of the human BRPF1 bromodomain in complex with SEED15
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Caflisch, A]]
+
<div class="pdbe-citations 5ev9" style="background-color:#fffaf0;"></div>
-
[[Category: Zhu, J]]
+
 
 +
==See Also==
 +
*[[Peregrin|Peregrin]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Caflisch A]]
 +
[[Category: Zhu J]]

Current revision

Crystal structure of the human BRPF1 bromodomain in complex with SEED15

PDB ID 5ev9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ev9"
Personal tools